Specificity and binding affinity of phospholipids to the high-affinity cardiolipin sites of beef heart cytochrome c oxidase

Biochemistry ◽  
1982 ◽  
Vol 21 (1) ◽  
pp. 184-188 ◽  
Author(s):  
Neal C. Robinson
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Binding Affinity ◽  
Beef Heart ◽  
High Affinity

scholarly journals Probing the high-affinity site of beef heart cytochrome c oxidase by cross-linking

1996 ◽  
Vol 315 (3) ◽  
pp. 909-916 ◽  
Author(s):  
Francesco MALATESTA ◽  
Giovanni ANTONINI ◽  
Flavia NICOLETTI ◽  
Alessandro GIUFFRÈ ◽  
Emilio D'ITRI ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Beef Heart ◽  
State Reduction ◽  
High Affinity ◽  
Disulphide Bond Formation ◽  
High Affinity Site ◽  
Low Ionic Strength ◽  
Covalent Complex

A covalent complex between cytochrome c oxidase and Saccharomyces cerevisiae iso-1-cytochrome c (called caa3) has been prepared at low ionic strength. Subunit III Cys-115 of beef heart cytochrome c oxidase cross-links by disulphide bond formation to thionitrobenzoate-modified yeast cytochrome c, a derivative shown to bind into the high-affinity site for substrate [Fuller, Darley-Usmar and Capaldi (1981) Biochemistry 20, 7046–7053]. Stopped-flow experiments show that (1) covalently bound yeast cytochrome c cannot donate electrons to cytochrome oxidase, whereas oxidation of exogenously added cytochrome c and electron transfer to cytochrome a are only slightly affected; (2) the steady-state reduction levels of cytochrome c and cytochrome a in the covalent complex caa3 are higher than those found in the native aa3 enzyme. However, (3) Km and Vmax values obtained from the non-linear Eadie–Hofstee plots are very similar in both caa3 and aa3. The results imply that cytochrome c bound to the high-affinity site is not in a configuration optimal for electron transfer.

scholarly journals Cloning and sequencing of the cDNA for a 13th different subunit (IHQ) of beef heart cytochrome c oxidase

1989 ◽  
Vol 264 (28) ◽  
pp. 16858-16861
Author(s):  
R Lightowlers ◽  
S Takamiya ◽  
R Wessling ◽  
M Lindorfer ◽  
R A Capaldi
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Beef Heart ◽  
Cloning And Sequencing

Reaction of thionitrobenzoate-modified yeast cytochrome c with monomeric and dimeric forms of beef heart cytochrome c oxidase

FEBS Letters ◽  
1984 ◽  
Vol 166 (1) ◽  
pp. 131-135 ◽  
Author(s):  
Victor M. Darley-Usmar ◽  
Gradimir Georgevich ◽  
Roderick A. Capaldi
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Beef Heart

Topology of beef heart cytochrome c oxidase from studies on reconstituted membranes

Biochemistry ◽  
1984 ◽  
Vol 23 (23) ◽  
pp. 5616-5621 ◽  
Author(s):  
Yu Zhong Zhang ◽  
Roderick A. Capaldi
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Beef Heart ◽  
Reconstituted Membranes

Arrangement of subunit IV in beef heart cytochrome c oxidase probed by chemical labeling and protease digestion experiments

Biochemistry ◽  
1983 ◽  
Vol 22 (19) ◽  
pp. 4405-4411 ◽  
Author(s):  
Francesco Malatesta ◽  
Victor Darley-Usmar ◽  
Catharina De Jong ◽  
Lawrence J. Prochaska ◽  
Roberto Bisson ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Beef Heart ◽  
Chemical Labeling ◽  
Protease Digestion

Comparative resonance Raman study of cytochrome c oxidase from beef heart and Paracoccus denitrificans

Biochemistry ◽  
1993 ◽  
Vol 32 (40) ◽  
pp. 10866-10877 ◽  
Author(s):  
George E. Heibel ◽  
Peter Hildebrandt ◽  
Bernd Ludwig ◽  
Peter Steinruecke ◽  
Tewfik Soulimane ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Paracoccus Denitrificans ◽  
Resonance Raman ◽  
Beef Heart ◽  
Raman Study
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